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1  of resident lipid transfer proteins, namely saposins.
2 tion site are strictly conserved in all four saposins.
3 me cases, by lipid transfer proteins such as saposins.
4 t sphingolipid-activating proteins (SAPs) or saposins.
5 ns into a critical cysteine in each of these saposins.
6                                   Individual saposin A (A-/-) and saposin B (B-/-)-deficient mice sho
7                                              Saposin A (SapA) lipoprotein discs, also known as picodi
8 the nonsignal NH2-terminal peptide preceding saposin A (termed Nter) was usually removed prior to sap
9 d saposins C and A, wild-type saposin C, and saposin A [Y30A], poorly with saposin C [A31Y], and not
10                     In the absence of lipid, saposin A adopts a closed monomeric apo conformation typ
11 osed of human sphingolipid activator protein saposin A and a small number of phospholipids, to displa
12                                              Saposin A and B proteins were undetectable in AB-/- mice
13              By site-directed mutagenesis of saposin A and C, their membrane topological structures w
14 nted using picodiscs (complexes comprised of saposin A and lipids, PDs), to screen mixtures of glycol
15 A (termed Nter) was usually removed prior to saposin A cleavage.
16                                              Saposin A contains an additional glycosylation site and
17 hat, in addition to GALC deficiency, genetic saposin A deficiency could also cause chronic GLD.
18                                      Genetic saposin A deficiency might be anticipated among human pa
19 genic activity whereas reduced and alkylated saposin A did.
20  an amino acid substitution (C106F) into the saposin A domain by the Cre/loxP system which eliminated
21                                    Wild-type saposin A had no neuritogenic activity whereas reduced a
22                                              Saposin A has roles in sphingolipid catabolism and trans
23          The structure reveals two chains of saposin A in an open conformation encapsulating 40 inter
24 tein, we determined the crystal structure of saposin A in the presence of detergent to 1.9 A resoluti
25                                        Thus, saposin A is indispensable for in vivo degradation of ga
26                                              Saposin A lipoprotein discs exhibit limited selectivity
27                         However, no specific saposin A or D deficiency is known.
28 on of saposin C, and the analogous region of saposin A showed that more "saposin C-like" molecules ha
29 ic placement of amino acids, and that Y30 of saposin A significantly alters local conformation in thi
30                Introduction of the conserved saposin A Tyr 30 (Y30) into saposin C at the analogous p
31  through a tetrasaposin, A-B-C-D, from which saposin A was then removed.
32                                 Nondenatured saposin A with an introduced A30 acquired substantial ne
33                   The phenotypic features of saposin A(-/-) mice are qualitatively identical but mild
34                                              Saposin A(-/-) mice developed slowly progressive hind le
35                                         When saposin A(-/-) mice were subcutaneously implanted with t
36                      During intercrossing of saposin A(-/-) mice, we observed that affected females t
37 ntly down-regulated in the brain of pregnant saposin A(-/-) mice.
38 s and microglia in the demyelinating area of saposin A(-/-) mice.
39  chronic form of the disease by inactivating saposin A, the essential activator of galactosylceramida
40                             Those with more "saposin A-like" spectra did not.
41 osin C [A31Y], and not at all with wild-type saposin A.
42  with amino acids in the analogous region of saposin A.
43        These findings indicate that combined saposins A and B deficiencies attenuated GalCer-beta-gal
44 created by knock-in point mutations into the saposins A and B domains on the prosaposin locus.
45 n insight into the interrelated functions of saposins A and B, combined saposin AB-deficient mice (AB
46 iencies of saposins C and D and decreases in saposins A and B.
47                                              Saposins A and C were produced in Escherichia coli to co
48 elices at the amino- and carboxyl termini of saposins A and C were shown to insert into the lipid bil
49 n models are proposed for the membrane-bound saposins A and C.
50          In comparison, the middle region of saposins A or C were either embedded in the bilayer or s
51                 In C-/- mice, prosaposin and saposins A, B and D proteins were present at near wild-t
52                                              Saposins A, B, C and D are derived from a common precurs
53             Sphingolipid activator proteins (saposins A, B, C and D) are small homologous glycoprotei
54 otein that encodes four glycoproteins, named saposins A, B, C and D.
55 precursor of four activator proteins, termed saposins A, B, C, and D, that are required for much of g
56                 Prosaposin, the precursor of saposins A, B, C, and D, was recently identified as a ne
57                 Prosaposin, the precursor of saposins A, B, C, and D, was recently reported to be a n
58 zygotes (B-/-) mice, whereas prosaposin, and saposins A, C and D were at normal levels.
59                                              Saposins (A, B, C and D) are approximately 80 amino acid
60                                              Saposins (A, B, C, and D) are small sphingolipid activat
61                                 Based on the saposin-A (SapA) scaffold protein, we demonstrate the su
62 ated functions of saposins A and B, combined saposin AB-deficient mice (AB-/-) were created by knock-
63                            Here we show that saposins, although not required for the autoreactive rec
64     We propose that MTP acts upstream of the saposins and functions as an ER chaperone by loading end
65 res are closely related, suggesting that all saposins and saposin-like domains share a common topolog
66                      Total deficiency of all saposins and specific deficiency of saposin B or C are k
67                      The oligosaccharides on saposins are not required for in vitro activation functi
68                                              Saposins are small, heat-stable glycoprotein activators
69                                          The saposins are small, membrane-active proteins that exist
70 r proteins SAP-A, -B, -C and -D (also called saposins) are generated by proteolytic processing from a
71              Individual saposin A (A-/-) and saposin B (B-/-)-deficient mice show unique phenotypes c
72                                              Saposin B (Sap B) is an essential activator protein for
73                             Recently, native saposin B (sapB) has been shown to bind CoQ10 and subseq
74 posins containing various length segments of saposin B and C localized the neurotrophic and acid beta
75          Patients with kidney disease lacked saposin B and showed new components in two patterns: the
76                                        Using saposin B as a unreactive backbone, chimeric saposins co
77                                We found that saposin B bound to neutral glycosphingolipids and gangli
78                                              Saposin B could also mediate lipid binding to soluble CD
79      Blocking sulfatide degradation from the saposin B deficiency diminished galactosylceramide accum
80                                              Saposin B derives from the multi-functional precursor, p
81 ng and compressing the central cavity of the saposin B dimer, may play a key role in facilitating lip
82        These findings delineate the roles of saposin B for the in vivo degradation of several GSLs an
83 ting a compensation in LacCer degradation by saposin B for the saposin C deficiency.
84                                We found that saposin B forms soluble saposin protein-lipid complexes
85 wed few components other than two ubiquitous saposin B glycoisoforms.
86 e of SDS is very similar to a monomer in the saposin B homodimer structure.
87  of B-/- mice supporting the in vivo role of saposin B in the degradation of these lipids.
88 ore assays we demonstrated that lipid-loaded saposin B increases the off-rate of lipids bound to CD1d
89                                              Saposin B is a water soluble alpha-helical protein which
90                       The X-ray structure of saposin B is homodimeric.
91 gher than that of lysosomes, suggesting that saposin B may facilitate lipid binding to CD1d molecules
92                                      Because saposin B must bind lipids directly to function, we foun
93 y of all saposins and specific deficiency of saposin B or C are known among human patients.
94                                 Mutations in saposin B present in humans with phenotypes resembling m
95                                           No saposin B protein was detected in the homozygotes (B-/-)
96  be absolutely essential, but the absence of saposin B resulted in the lowest recognition of alpha-ga
97                                              Saposin B was also the most efficient in mediating alpha
98 were added to the prosaposin-negative cells, saposin B was the most efficient in restoring CD1d recog
99                         To gain insight into saposin B's physiological functions, a specific deficien
100 lex formation between glycosphingolipids and saposin B, a separate activator protein with broad speci
101                                   Similar to saposin B, NPC2 dimers were able to load isoglobotrihexo
102 ort (5 ns) molecular dynamics simulations of saposin B, starting from both the AB and CD conformation
103                           The optimal pH for saposin B-mediated lipid binding to CD1d, pH 6, is highe
104                               Three of these saposins (B, C, and D) share common structural features
105 d by creating mice with selective absence of saposin C (C-/-) using a knock-in point mutation (cystei
106                                              Saposin C (Sap C) is a small glycoprotein required for h
107                           The interaction of Saposin C (Sap C) with negatively charged phospholipids
108                                              Saposin C (Trp-free) induced additional activity and flu
109 saposin C, and saposin A [Y30A], poorly with saposin C [A31Y], and not at all with wild-type saposin
110                                              Saposin C adopts the saposin-fold common to other member
111                CD spectral changes indicated saposin C and acid beta-glucosidase interaction only in
112                          The CD-/- mice with saposin C and D combined deficiencies were produced by i
113 e curves demonstrated maximal enhancement by saposin C and prosaptides at low nanomolar concentration
114 etectable in AB-/- mice, whereas prosaposin, saposin C and saposin D were expressed near wild-type (W
115 of the conserved saposin A Tyr 30 (Y30) into saposin C at the analogous position 31, a conserved Ala(
116 s the first representation of membrane bound saposin C at the atomic level.
117 induces essential conformational changes for saposin C binding and further enhancement of acid beta-g
118                                              Saposin C binds to membranes to activate lipid degradati
119 phospholipids or, particularly, phospholipid/saposin C complexes by intrinsic fluorescence spectral s
120 ibodies directed against the NH2-terminus of saposin C cross-reacted well with reduced and alkylated
121                        The few patients with saposin C deficiency develop a Gaucher disease-like cent
122 n in LacCer degradation by saposin B for the saposin C deficiency.
123 t the in vivo effects of saposin C on GCase, saposin C deficient mice (C-/-) were backcrossed to poin
124 the membrane-binding behavior of a mutant of saposin C designed to decrease the negative charge of th
125 lized to a 12-amino acid sequence within the saposin C domain and has been used to derive biologicall
126 ing the neurotrophic sequence located in the saposin C domain.
127                                  Deficits in saposin C enhancement of k(cat) were present in variant
128                                 In contrast, saposin C facilitates CD1 lipid loading in a different w
129 hway, acid beta-glucosidase (GCase) requires saposin C for optimal in vitro and in vivo hydrolysis of
130          These results support the view that saposin C has multiple roles in glycosphingolipid (GSL)
131               In addition, the deficiency of saposin C in CD-/- mice resulted in cellular decreases o
132 st, the previously reported NMR structure of saposin C in the absence of SDS is compact and contains
133                             The structure of saposin C in the presence of SDS is very similar to a mo
134  the three-dimensional solution structure of saposin C in the presence of the detergent sodium dodecy
135                    Conformational changes of saposin C induced by phosphatidylserine interaction sugg
136                                        Since saposin C is a lysosomal protein and pH gradients occur
137                                              Saposin C is a lysosomal protein needed for optimal GCas
138                                              Saposin C is a lysosomal, membrane-binding protein that
139                                              Saposin C is an essential co-factor for the hydrolysis o
140                     These data indicate that saposin C is required for GCase resistance to proteolyti
141                               The absence of saposin C led to moderate increases in GC and lactosylce
142  negatively charged electrostatic surface of saposin C needs to be partially neutralized to trigger m
143               To test the in vivo effects of saposin C on GCase, saposin C deficient mice (C-/-) were
144 re present at near wild-type levels, but the saposin C protein was absent.
145                         Across species, this saposin C region has a high degree of identity and simil
146 udies show that the neuritogenic activity of saposin C requires specific placement of amino acids, an
147                                      Loading saposin C to human PS-/- fibroblasts resulted in an enha
148                  We find that the binding of saposin C to phospholipid vesicles is a pH-controlled re
149  proper orientation of the middle segment of saposin C to the outside of the membrane surface is crit
150 nesis localized the activation properties of saposin C to the region spanning residues 47-62.
151 of neurotrophic and activation properties of saposin C to two different faces of the molecule and sug
152 se neurotrophic and activation properties of saposin C was elucidated using recombinant or chemically
153            Of the four mature saposins, only saposin C was found to increase sulfatide concentrations
154                       The in vivo effects of saposin C were examined by creating mice with selective
155                         To get insights into saposin C's function, we have determined its three-dimen
156 the lysosome could be switched on and off by saposin C's reversible binding to membranes.
157 f the pure enzyme requires phospholipids and saposin C, an 80 aa activator protein.
158    These results indicate a new property for saposin C, an anti-proteolytic protective function towar
159 ed and alkylated saposins C and A, wild-type saposin C, and saposin A [Y30A], poorly with saposin C [
160  A, the corresponding neuritogenic region of saposin C, and the analogous region of saposin A showed
161 ies to the carboxyl- and NH2-terminal 50% of saposin C, respectively.
162 logous region of saposin A showed that more "saposin C-like" molecules had neuritogenic properties.
163 ed only from the lack of GCase activation by saposin C.
164 is localized to amino acid residues 22-31 of saposin C.
165  neurite outgrowth in vitro via sequences in saposin C.
166 resented at acidic pH and in the presence of saposin C.
167                         Wild-type and mutant saposins C and A from human and mouse were expressed in
168           CD spectra of wild-type and mutant saposins C and A, the corresponding neuritogenic region
169 ross-reacted well with reduced and alkylated saposins C and A, wild-type saposin C, and saposin A [Y3
170 paired prosaposin secretion, deficiencies of saposins C and D and decreases in saposins A and B.
171 r T (iNKT) cells, it remains unclear whether saposins can facilitate loading of endogenous iNKT cell
172 saposin B as a unreactive backbone, chimeric saposins containing various length segments of saposin B
173  using recombinant or chemically synthesized saposin Cs from various regions of the molecule.
174 he complement of disulfide bonds in selected saposin Cs.
175                                              Saposin D loading had no effect.
176 B-/- mice, whereas prosaposin, saposin C and saposin D were expressed near wild-type (WT) levels.
177          In both humans and mice, prosaposin/saposin deficiencies lead to severe neurological deficit
178                       A mouse model of total saposin deficiency closely mimics the human disease.
179                                              Saposins, derived from a common precursor, prosaposin, a
180 embrane interactions and orientations of the saposins determine the proximity of their activation and
181 Both contain a signal sequence followed by a saposin domain and a GDSL-lipase domain.
182                                    In vitro, saposins extracted monomeric lipids from membranes and f
183                                              Saposins facilitate this process, but the mechanisms use
184  transfer proteins, such as molecules of the saposin family, facilitate extraction of lipids from bio
185 mprised of four alpha-helices that adopt the saposin fold, characteristic of a protein family that bi
186                         Saposin C adopts the saposin-fold common to other members of the family.
187 elical bundle of granulysin resembles other "saposin folds" (such as NK-lysin).
188 ic reticulum is complementary to that of the saposins in endosomes in vivo.
189 plore the in vivo functional interactions of saposins in GSL metabolism and lysosomal storage disease
190 eate the tissue differential interactions of saposins in GSL metabolism.
191 osaposin deletion mutants lacking individual saposins in prosaposin-negative, CD1d-positive cells.
192           In addition, it is unclear whether saposins, in addition to loading, also promote dissociat
193 ion of cellular assays and demonstrated that saposins influence CD1d-restricted presentation to human
194                             To determine the saposins involved in promoting lipid binding to CD1d, we
195 ighlight critical but different roles of the saposin-like and cytokine-like domains, including the th
196  cysteine mutations in the amino part of the saposin-like domain and in the base of the index finger
197 peptide SP-B(N), derived from the N-terminal saposin-like domain of the surfactant protein (SP)-B pro
198              The conserved regions include a saposin-like domain, proline-rich domain, and a putative
199 ly related, suggesting that all saposins and saposin-like domains share a common topology.
200                      SP-B is a member of the saposin-like family of proteins, several of which have a
201 nment of deduced J3-crystallin indicates two saposin-like motifs arranged in tandem, each containing
202 xpression of Canopy2 (Cnpy2)/MIR-interacting Saposin-like protein (Msap) that is known to interact wi
203 t protein B (SP-B) proprotein contains three saposin-like protein (SAPLIP) domains: a SAPLIP domain c
204 ilarity to the homologous regions of related saposin-like proteins and the importance of the distribu
205 intramolecular disulfide bonds shared by all saposin-like proteins.
206 omain with NK-lysin indicates that these two saposin-like structures are closely related, suggesting
207 ading lipid antigens without forming soluble saposin-lipid antigen complexes.
208                            Here we present a saposin-lipoprotein nanoparticle system, Salipro, which
209                              We suggest that saposins mobilize monomeric lipids from lysosomal membra
210       Exon 3 encodes a circularly permutated saposin motif, called a swaposin, found in plant asparti
211 bumins, nonspecific lipid transfer proteins, saposins, nematode polyprotein allergens/antigens).
212                           Of the four mature saposins, only saposin C was found to increase sulfatide
213 ivery of prosaposin (PSAP), the precursor of saposin peptides that are essential for lysosomal glycos
214 st a crystallin role for the multifunctional saposin protein family in the jellyfish lens.
215        We found that saposin B forms soluble saposin protein-lipid complexes detected by native gel e
216 ironment that is stabilized by a scaffold of saposin proteins.
217                                No individual saposin proved to be absolutely essential, but the absen
218                 The deficiency of prosaposin/saposins (PS-/-) in humans and mice leads to a decrease
219 he lipid antigen loading machinery genes pro-saposin (Psap), Niemann Pick type C2 (Npc2), alpha-galac
220   Importantly, we determined that similar to saposins, recombinant NPC2 was able to unload lipids fro
221 s and indicates that the putative primordial saposin/swaposin J3-crystallin reflects both the chapero
222 , in tandem, four glycoprotein activators or saposins, termed A, B, C, and D, that are essential for
223 espite high sequence homology among the four saposins, they have different specificities for lipid su
224  for understanding the contributions of this saposin to GSL metabolism and homeostasis.
225  tuned over a wide pH range by adjusting the saposin-to-lipid stoichiometry, enabling maintenance of
226                    These findings reveal how saposins use different strategies to facilitate transfer
227                   When recombinant exogenous saposins were added to the prosaposin-negative cells, sa
228               We hypothesized that lysosomal saposins, which are cofactors required for sphingolipid
229  cystophora), shows similarity to vertebrate saposins, which are multifunctional proteins that bridge

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